ID F4P2T6_BATDJ Unreviewed; 797 AA.
AC F4P2T6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Multifunctional tryptophan biosynthesis protein {ECO:0000256|ARBA:ARBA00018819};
DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
DE EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572};
GN ORFNames=BATDEDRAFT_88876 {ECO:0000313|EMBL:EGF80078.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF80078.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF80078.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase
CC (GATase) domain of anthranilate synthase, indole-glycerolphosphate
CC synthase, and phosphoribosylanthranilate isomerase activities.
CC {ECO:0000256|ARBA:ARBA00003272}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000256|ARBA:ARBA00001164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000256|ARBA:ARBA00000329};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL882884; EGF80078.1; -; Genomic_DNA.
DR RefSeq; XP_006679160.1; XM_006679097.1.
DR AlphaFoldDB; F4P2T6; -.
DR STRING; 684364.F4P2T6; -.
DR MEROPS; C26.A25; -.
DR GeneID; 18243307; -.
DR HOGENOM; CLU_007713_2_0_1; -.
DR InParanoid; F4P2T6; -.
DR OMA; EPIEWAN; -.
DR OrthoDB; 294181at2759; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 2.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 4..186
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 254..516
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 539..588
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT DOMAIN 615..793
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 797 AA; 85494 MW; 97D82DC47FF20F28 CRC64;
MTTLLIDNYD SFTWNVYQLL SELGANVKVV RNDLITIDEA IRLNPRNVVI SPGPGHPSTA
GISNDIIRHF AGLIPILGVC LGEQCIYEIY GGTVSRVGEL VHGKTTQVMH DGLYLYDGVP
QNIECTRYHS LAGTLDTLPD VLTITARTAS GVIMGVRHND LVMEGVQFHP ESIASESGRK
LFANFLSWEG GHWSSLKIKA HLVNYDEATE LNRVASAASY PGVGNGIPLS AITKLNSTSK
SVTTTATGPS ENILEKITRQ RKRDVVADMT KPGCSFLHLQ RSIALGLAPI AINFKDRLVQ
NDQGQVAVLA EIKRASPSKG DICPSAHAAT IAQTYAVSGA SAISVLTEPT WFKGSLSDML
QARLAVQHIT NRPAILCKDF IIDRYQILQA RLHGADTLLL IVACLTDDQL LSLMSFSRQL
GMEPLVEVAS AEEMQRAVKL GSQVIGVNNR DLKTFSVDTS RTTELASMVP SDVVLIALSG
ITCRRDIEPY LAAGARGVLV GEALMKASNK HAFIGSLADP SIPYSESFQS ASMAHSQRVK
ICGITNTKDA IAAVDAGADF LGLIFASSSA RRVDATQAAE IVLSVRKETN THRSVTPFSR
VLATSFPTYA SHTMNASPEA WFMSRATDGV LPRRTPLFVG VFTTQSASEI QSIVDTVGLD
LVQMHNATPD PDLPALISVP TIQVLHVDPT TTGEALLQQI SSFSHRASFI LLDTSAAAGS
GSGGSGQVFD WSVAKKISAL KIPFFLAGGL CSNNVSEAVS TAQPWCVDVC SGVEMEGKKG
IKDESLMQLF VKNAAFR
//
